2MBD
Lasiocepsin
Summary for 2MBD
| Entry DOI | 10.2210/pdb2mbd/pdb |
| NMR Information | BMRB: 19396 |
| Descriptor | lasiocepsin (1 entity in total) |
| Functional Keywords | antimicrobial peptide, wild bee, venom, antimicrobial protein |
| Biological source | Lasioglossum laticeps (bees) |
| Total number of polymer chains | 1 |
| Total formula weight | 2906.84 |
| Authors | Monincova, L.,Budesinsky, M.,Cujova, S.,Cerovsky, V.,Veverka, V. (deposition date: 2013-07-30, release date: 2014-01-15, Last modification date: 2024-10-30) |
| Primary citation | Monincova, L.,Budesinsky, M.,Cujova, S.,Cerovsky, V.,Veverka, V. Structural basis for antimicrobial activity of lasiocepsin. Chembiochem, 15:301-308, 2014 Cited by PubMed Abstract: Lasiocepsin is a unique 27-residue antimicrobial peptide, isolated from Lasioglossum laticeps (wild bee) venom, with substantial antibacterial and antifungal activity. It adopts a well-defined structure consisting of two α-helices linked by a structured loop. Its basic residues form two distinct positively charged regions on the surface whereas aliphatic side chains contribute to solvent-accessible hydrophobic areas, thus emphasising the amphipathic character of the molecule. Lasiocepsin structurally belongs to the ShK family and shows a strong preference for anionic phospholipids; this is further augmented by increasing concentrations of cardiolipin, such as those found at the poles of bacterial cells. The membrane-permeabilising activity of the peptide is not limited to outer membranes of Gram-negative bacteria. The peptide interacts with phospholipids initially through its N terminus, and its degree of penetration is strongly dependent on the presence of cardiolipin. PubMed: 24339323DOI: 10.1002/cbic.201300509 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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